UniProt ID | PGM2_YEAST | |
---|---|---|
UniProt AC | P37012 | |
Protein Name | Phosphoglucomutase 2 {ECO:0000303|PubMed:5784209} | |
Gene Name | PGM2 {ECO:0000303|PubMed:5784209} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 569 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. [PubMed: 5784209 Constitutes about 80-90% of the phosphoglucomutase activity in the cell] | |
Protein Sequence | MSFQIETVPTKPYEDQKPGTSGLRKKTKVFKDEPNYTENFIQSIMEAIPEGSKGATLVVGGDGRYYNDVILHKIAAIGAANGIKKLVIGQHGLLSTPAASHIMRTYEEKCTGGIILTASHNPGGPENDMGIKYNLSNGGPAPESVTNAIWEISKKLTSYKIIKDFPELDLGTIGKNKKYGPLLVDIIDITKDYVNFLKEIFDFDLIKKFIDNQRSTKNWKLLFDSMNGVTGPYGKAIFVDEFGLPADEVLQNWHPSPDFGGMHPDPNLTYASSLVKRVDREKIEFGAASDGDGDRNMIYGYGPSFVSPGDSVAIIAEYAAEIPYFAKQGIYGLARSFPTSGAIDRVAKAHGLNCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHVREKDGVWAIMAWLNILAIYNKHHPENEASIKTIQNEFWAKYGRTFFTRYDFEKVETEKANKIVDQLRAYVTKSGVVNSAFPADESLKVTDCGDFSYTDLDGSVSDHQGLYVKLSNGARFVLRLSGTGSSGATIRLYIEKYCDDKSQYQKTAEEYLKPIINSVIKFLNFKQVLGTEEPTVRT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSFQIETVP ------CCCEEEECC | 26.34 | 22369663 | |
2 | Acetylation | ------MSFQIETVP ------CCCEEEECC | 26.34 | 22814378 | |
13 | Phosphorylation | ETVPTKPYEDQKPGT EECCCCCCCCCCCCC | 33.42 | 22369663 | |
20 | Phosphorylation | YEDQKPGTSGLRKKT CCCCCCCCCCCCHHC | 28.31 | 22369663 | |
21 | Phosphorylation | EDQKPGTSGLRKKTK CCCCCCCCCCCHHCE | 41.57 | 22369663 | |
95 | Phosphorylation | IGQHGLLSTPAASHI ECCCCCCCCHHHHHH | 37.07 | 22369663 | |
96 | Phosphorylation | GQHGLLSTPAASHIM CCCCCCCCHHHHHHH | 19.54 | 22369663 | |
100 | Phosphorylation | LLSTPAASHIMRTYE CCCCHHHHHHHHHHH | 18.69 | 22369663 | |
111 | Phosphorylation | RTYEEKCTGGIILTA HHHHHHCCCEEEEEC | 49.89 | 22890988 | |
117 | Phosphorylation | CTGGIILTASHNPGG CCCEEEEECCCCCCC | 18.73 | 22369663 | |
119 | Phosphorylation | GGIILTASHNPGGPE CEEEEECCCCCCCCC | 20.68 | 25521595 | |
129 | Oxidation | PGGPENDMGIKYNLS CCCCCCCCCCEEECC | 10.10 | 15665377 | |
155 | 2-Hydroxyisobutyrylation | AIWEISKKLTSYKII HHHHHHHHHHCCCCC | 50.65 | - | |
160 | 2-Hydroxyisobutyrylation | SKKLTSYKIIKDFPE HHHHHCCCCCCCCCC | 37.41 | - | |
163 | Acetylation | LTSYKIIKDFPELDL HHCCCCCCCCCCCCC | 57.71 | 24489116 | |
289 | Phosphorylation | KIEFGAASDGDGDRN HCEECCCCCCCCCCC | 41.41 | 28889911 | |
428 | 2-Hydroxyisobutyrylation | IQNEFWAKYGRTFFT HHHHHHHHHCCCEEE | 38.54 | - | |
428 | Acetylation | IQNEFWAKYGRTFFT HHHHHHHHHCCCEEE | 38.54 | 24489116 | |
437 | Phosphorylation | GRTFFTRYDFEKVET CCCEEECCCHHHHCH | 23.17 | 27017623 | |
441 | Acetylation | FTRYDFEKVETEKAN EECCCHHHHCHHHHH | 45.42 | 24489116 | |
444 | Phosphorylation | YDFEKVETEKANKIV CCHHHHCHHHHHHHH | 45.86 | 27017623 | |
446 | Acetylation | FEKVETEKANKIVDQ HHHHCHHHHHHHHHH | 65.76 | 24489116 | |
449 | Acetylation | VETEKANKIVDQLRA HCHHHHHHHHHHHHH | 49.30 | 24489116 | |
512 | Phosphorylation | ARFVLRLSGTGSSGA CEEEEEECCCCCCCC | 28.07 | 30377154 | |
514 | Phosphorylation | FVLRLSGTGSSGATI EEEEECCCCCCCCEE | 30.43 | 30377154 | |
516 | Phosphorylation | LRLSGTGSSGATIRL EEECCCCCCCCEEEE | 25.99 | 22369663 | |
517 | Phosphorylation | RLSGTGSSGATIRLY EECCCCCCCCEEEEE | 33.52 | 22369663 | |
520 | Phosphorylation | GTGSSGATIRLYIEK CCCCCCCEEEEEEHH | 15.34 | 22369663 | |
527 | Acetylation | TIRLYIEKYCDDKSQ EEEEEEHHHCCCHHH | 41.44 | 24489116 | |
535 | Phosphorylation | YCDDKSQYQKTAEEY HCCCHHHHHHHHHHH | 21.04 | 25533186 | |
537 | Acetylation | DDKSQYQKTAEEYLK CCHHHHHHHHHHHHH | 44.78 | 22865919 | |
544 | Succinylation | KTAEEYLKPIINSVI HHHHHHHHHHHHHHH | 33.01 | 23954790 | |
544 | Acetylation | KTAEEYLKPIINSVI HHHHHHHHHHHHHHH | 33.01 | 24489116 | |
557 | Acetylation | VIKFLNFKQVLGTEE HHHHCCHHHHHCCCC | 38.12 | 24489116 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PGM2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PGM2_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PGM2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117 AND SER-119, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY. |